M. L. Standaert

Protein kinase C-lambda knockout in embryonic stem cells and adipocytes impairs insulin-stimulated glucose transport (2004)

Bandyopadhyay,G., Standaert,M. L., Sajan,M. P., Kanoh,Y., Miura,A., Braun,U., ...

Atypical protein kinase C (aPKC) isoforms have been suggested to mediate insulin effects on glucose transport in adipocytes and other cells. To more rigorously test this hypothesis, we generated...

Protein kinase C-lambda knockout in embryonic stem cells and adipocytes impairs insulin-stimulated glucose transport (2004)

Bandyopadhyay, G., Standaert, M. L., Sajan, M. P., Kanoh, Y., Miura, A., Braun, U., ...

Atypical protein kinase C (aPKC) isoforms have been suggested to mediate insulin effects on glucose transport in adipocytes and other cells. To more rigorously test this hypothesis, we generated...

Protein kinase C-lambda knockout in embryonic stem cells and adipocytes impairs insulin-stimulated glucose transport (2004)

Bandyopadhyay, G., Standaert, M. L., Sajan, M. P., Kanoh, Y., Miura, A., Braun, U., ...

Atypical protein kinase C (aPKC) isoforms have been suggested to mediate insulin effects on glucose transport in adipocytes and other cells. To more rigorously test this hypothesis, we generated...

Knock-out of protein kinase C-α enhances signaling through phosphatidylinositol 3-kinase. (2002)

Leitges,M., Plomann,M., Standaert,M. L., Bandyopadhyay,G., Sajan,M. P., Kanoh,Y., ...

Knock-out of protein kinase C-α enhances signaling through phosphatidylinositol 3-kinase. (2002)

Leitges, M., Plomann, M., Standaert, M. L., Bandyopadhyay, G., Sajan, M. P., Kanoh, Y., ...

Insulin-induced activation of glycerol-3-phosphate acyltransferase by a chiro-inositol-containing insulin mediator is defective in adipocytes of insulin-resistant, type II diabetic, Goto-Kakizaki rats.

Farese, R V, Standaert, M L, Yamada, K, Huang, L C, Zhang, C, Cooper, D R, ...

Type II diabetic Goto-Kakizaki (GK) rats were insulin-resistant in euglycemic-hyperinsulinemic clamp studies. We therefore examined insulin signaling systems in control Wistar and diabetic GK rats....

Preferential activation of microsomal diacylglycerol/protein kinase C signaling during glucose treatment (De Novo phospholipid synthesis) of rat adipocytes.

Farese, R V, Standaert, M L, Arnold, T P, Yamada, K, Musunuru, K, Hernandez, H, ...

Glucose has been reported to increase the de novo synthesis of diacylglycerol (DAG) and translocate and activate protein kinase C (PKC) in rat adipocytes. Presently, we examined the major subcellular...

Hormone-receptor interactions are noncooperative: application to the beta-adrenergic receptor.

Pollet, R J, Standaert, M L, Haase, B A

We have developed kinetic methods with which we have demonstrated that the negatively cooperative hormone-binding model is untenable for the insulin receptor system. These methods have led others to...

Effects of insulin and phorbol esters on subcellular distribution of protein kinase C isoforms in rat adipocytes.

Farese, R V, Standaert, M L, Francois, A J, Ways, K, Arnold, T P, Hernandez, H, ...

Effects of insulin and phorbol esters on subcellular distribution of protein kinase C (PKC) isoforms were examined in rat adipocytes. Both agonists provoked rapid decreases in cytosolic, and/or...

Effects of insulin and phorbol esters on MARCKS (myristoylated alanine-rich C-kinase substrate) phosphorylation (and other parameters of protein kinase C activation) in rat adipocytes, rat soleus muscle and BC3H-1 myocytes.

Arnold, T P, Standaert, M L, Hernandez, H, Watson, J, Mischak, H, Kazanietz, M G, ...

To evaluate the question of whether or not insulin activates protein kinase C (PKC), we compared the effects of insulin and phorbol esters on the phosphorylation of the PKC substrate, i.e....

Mechanisms whereby insulin increases diacylglycerol in BC3H-1 myocytes.

Farese, R V, Cooper, D R, Konda, T S, Nair, G, Standaert, M L, Davis, J S, ...

We previously suggested that insulin increases diacylglycerol (DAG) in BC3H-1 myocytes, both by increases in synthesis de novo of phosphatidic acid (PA) and by hydrolysis of non-inositol-containing...

Insulin provokes co-ordinated increases in the synthesis of phosphatidylinositol, phosphatidylinositol phosphates and the phosphatidylinositol-glycan in BC3H-1 myocytes.

Farese, R V, Cooper, D R, Konda, T S, Nair, G, Standaert, M L, Pollet, R J

BC3H-1 myocytes were cultured in the presence of [3H]inositol or [3H]glucosamine during their entire growth cycle to ensure that all lipids containing inositol and glucosamine were labelled to...

Effects of insulin on the translocation of protein kinase C-theta and other protein kinase C isoforms in rat skeletal muscles.

Yamada, K, Avignon, A, Standaert, M L, Cooper, D R, Spencer, B, Farese, R V

Protein kinase C (PKC)-theta is a newly recognized major PKC isoform in skeletal muscle. In this study we found that insulin provoked rapid biphasic increases in membrane-associated immunoreactive...

Insulin increases mRNA levels of protein kinase C-alpha and -beta in rat adipocytes and protein kinase C-alpha, -beta and -theta in rat skeletal muscle.

Avignon, A, Standaert, M L, Yamada, K, Mischak, H, Spencer, B, Farese, R V

Effects of insulin of levels of mRNA encoding protein kinase C (PKC)-alpha, PKC-beta, PKC-epsilon and PKC-theta were examined by ribonuclease protection assay in primary cultures of rat adipocytes in...

Insulin-like effects of epidermal growth factor and insulin-like growth factor-I on [3H]2-deoxyglucose uptake, diacylglycerol generation and protein kinase C activation in BC3H-1 myocytes.

Farese, R V, Nair, G P, Sierra, C G, Standaert, M L, Pollet, R J, Cooper, D R

Epidermal growth factor (EGF) and insulin-like growth factor-I (IGF-I) were found to provoke increases in [3H]2-deoxyglucose uptake, diacylglycerol (DAG) generation and membrane-bound protein kinase...

The de novo phospholipid effect of insulin is associated with increases in diacylglycerol, but not inositol phosphates or cytosolic Ca2+.

Farese, R V, Davis, J S, Barnes, D E, Standaert, M L, Babischkin, J S, Hock, R, ...

We have previously reported that insulin increases the synthesis de novo of phosphatidic acid (PA), phosphatidylinositol (PI), phosphatidylinositol 4-phosphate (PIP), phosphatidylinositol...

The phosphatidylinositol 3-kinase inhibitor, wortmannin, inhibits insulin-induced activation of phosphatidylcholine hydrolysis and associated protein kinase C translocation in rat adipocytes.

Standaert, M L, Avignon, A, Yamada, K, Bandyopadhyay, G, Farese, R V

We questioned whether phosphatidylinositol 3-kinase (PI 3-kinase) and protein kinase C (PKC) function as interrelated signalling mechanisms during insulin action in rat adipocytes. Insulin rapidly...

Effects of transiently expressed atypical (zeta, lambda), conventional (alpha, beta) and novel (delta, epsilon) protein kinase C isoforms on insulin-stimulated translocation of epitope-tagged GLUT4 glucose transporters in rat adipocytes: specific interchangeable effects of protein kinases C-zeta and C-lambda.

Bandyopadhyay, G, Standaert, M L, Kikkawa, U, Ono, Y, Moscat, J, Farese, R V

Atypical protein kinase (PK)C isoforms, zeta and lambda, have been reported to be activated by insulin via phosphoinositide 3-kinase, and have been suggested to be required for insulin-stimulated...

Insulin-induced activation of glycerol-3-phosphate acyltransferase by a chiro-inositol-containing insulin mediator is defective in adipocytes of insulin-resistant, type II diabetic, Goto-Kakizaki rats.

Farese, R V, Standaert, M L, Yamada, K, Huang, L C, Zhang, C, Cooper, D R, ...

Type II diabetic Goto-Kakizaki (GK) rats were insulin-resistant in euglycemic-hyperinsulinemic clamp studies. We therefore examined insulin signaling systems in control Wistar and diabetic GK rats....

Preferential activation of microsomal diacylglycerol/protein kinase C signaling during glucose treatment (De Novo phospholipid synthesis) of rat adipocytes.

Farese, R V, Standaert, M L, Arnold, T P, Yamada, K, Musunuru, K, Hernandez, H, ...

Glucose has been reported to increase the de novo synthesis of diacylglycerol (DAG) and translocate and activate protein kinase C (PKC) in rat adipocytes. Presently, we examined the major subcellular...

Hormone-receptor interactions are noncooperative: application to the beta-adrenergic receptor.

Pollet, R J, Standaert, M L, Haase, B A

We have developed kinetic methods with which we have demonstrated that the negatively cooperative hormone-binding model is untenable for the insulin receptor system. These methods have led others to...

Effects of insulin and phorbol esters on subcellular distribution of protein kinase C isoforms in rat adipocytes.

Farese, R V, Standaert, M L, Francois, A J, Ways, K, Arnold, T P, Hernandez, H, ...

Effects of insulin and phorbol esters on subcellular distribution of protein kinase C (PKC) isoforms were examined in rat adipocytes. Both agonists provoked rapid decreases in cytosolic, and/or...

Effects of insulin and phorbol esters on MARCKS (myristoylated alanine-rich C-kinase substrate) phosphorylation (and other parameters of protein kinase C activation) in rat adipocytes, rat soleus muscle and BC3H-1 myocytes.

Arnold, T P, Standaert, M L, Hernandez, H, Watson, J, Mischak, H, Kazanietz, M G, ...

To evaluate the question of whether or not insulin activates protein kinase C (PKC), we compared the effects of insulin and phorbol esters on the phosphorylation of the PKC substrate, i.e....

Mechanisms whereby insulin increases diacylglycerol in BC3H-1 myocytes.

Farese, R V, Cooper, D R, Konda, T S, Nair, G, Standaert, M L, Davis, J S, ...

We previously suggested that insulin increases diacylglycerol (DAG) in BC3H-1 myocytes, both by increases in synthesis de novo of phosphatidic acid (PA) and by hydrolysis of non-inositol-containing...

Insulin provokes co-ordinated increases in the synthesis of phosphatidylinositol, phosphatidylinositol phosphates and the phosphatidylinositol-glycan in BC3H-1 myocytes.

Farese, R V, Cooper, D R, Konda, T S, Nair, G, Standaert, M L, Pollet, R J

BC3H-1 myocytes were cultured in the presence of [3H]inositol or [3H]glucosamine during their entire growth cycle to ensure that all lipids containing inositol and glucosamine were labelled to...

Effects of insulin on the translocation of protein kinase C-theta and other protein kinase C isoforms in rat skeletal muscles.

Yamada, K, Avignon, A, Standaert, M L, Cooper, D R, Spencer, B, Farese, R V

Protein kinase C (PKC)-theta is a newly recognized major PKC isoform in skeletal muscle. In this study we found that insulin provoked rapid biphasic increases in membrane-associated immunoreactive...

Insulin increases mRNA levels of protein kinase C-alpha and -beta in rat adipocytes and protein kinase C-alpha, -beta and -theta in rat skeletal muscle.

Avignon, A, Standaert, M L, Yamada, K, Mischak, H, Spencer, B, Farese, R V

Effects of insulin of levels of mRNA encoding protein kinase C (PKC)-alpha, PKC-beta, PKC-epsilon and PKC-theta were examined by ribonuclease protection assay in primary cultures of rat adipocytes in...

Insulin-like effects of epidermal growth factor and insulin-like growth factor-I on [3H]2-deoxyglucose uptake, diacylglycerol generation and protein kinase C activation in BC3H-1 myocytes.

Farese, R V, Nair, G P, Sierra, C G, Standaert, M L, Pollet, R J, Cooper, D R

Epidermal growth factor (EGF) and insulin-like growth factor-I (IGF-I) were found to provoke increases in [3H]2-deoxyglucose uptake, diacylglycerol (DAG) generation and membrane-bound protein kinase...

The de novo phospholipid effect of insulin is associated with increases in diacylglycerol, but not inositol phosphates or cytosolic Ca2+.

Farese, R V, Davis, J S, Barnes, D E, Standaert, M L, Babischkin, J S, Hock, R, ...

We have previously reported that insulin increases the synthesis de novo of phosphatidic acid (PA), phosphatidylinositol (PI), phosphatidylinositol 4-phosphate (PIP), phosphatidylinositol...

The phosphatidylinositol 3-kinase inhibitor, wortmannin, inhibits insulin-induced activation of phosphatidylcholine hydrolysis and associated protein kinase C translocation in rat adipocytes.

Standaert, M L, Avignon, A, Yamada, K, Bandyopadhyay, G, Farese, R V

We questioned whether phosphatidylinositol 3-kinase (PI 3-kinase) and protein kinase C (PKC) function as interrelated signalling mechanisms during insulin action in rat adipocytes. Insulin rapidly...

Effects of transiently expressed atypical (zeta, lambda), conventional (alpha, beta) and novel (delta, epsilon) protein kinase C isoforms on insulin-stimulated translocation of epitope-tagged GLUT4 glucose transporters in rat adipocytes: specific interchangeable effects of protein kinases C-zeta and C-lambda.

Bandyopadhyay, G, Standaert, M L, Kikkawa, U, Ono, Y, Moscat, J, Farese, R V

Atypical protein kinase (PK)C isoforms, zeta and lambda, have been reported to be activated by insulin via phosphoinositide 3-kinase, and have been suggested to be required for insulin-stimulated...